(data stored in SCRATCH zone)

SWISSPROT: ECH1_RAT

ID   ECH1_RAT                Reviewed;         327 AA.
AC   Q62651;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   30-AUG-2017, entry version 136.
DE   RecName: Full=Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial;
DE            EC=5.3.3.-;
DE   Flags: Precursor;
GN   Name=Ech1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=7558027; DOI=10.1006/geno.1995.1077;
RA   Fitzpatrick D.R., Germain-Lee E., Valle D.;
RT   "Isolation and characterization of rat and human cDNAs encoding a
RT   novel putative peroxisomal enoyl-CoA hydratase.";
RL   Genomics 27:457-466(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 185-210 AND 219-229, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (NOV-2006) to UniProtKB.
RN   [4]
RP   CHARACTERIZATION.
RC   TISSUE=Liver;
RX   PubMed=9417087; DOI=10.1074/jbc.273.1.349;
RA   Filppula S.A., Yagi A.I., Kilpeleainen S.H., Novikov D.,
RA   Fitzpatrick D.R., Vihinen M., Valle D., Hiltunen J.K.;
RT   "Delta3,5-delta2,4-dienoyl-CoA isomerase from rat liver. Molecular
RT   characterization.";
RL   J. Biol. Chem. 273:349-355(1998).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SEQUENCE REVISION TO 164, AND
RP   SUBUNIT.
RX   PubMed=9739087; DOI=10.1016/S0969-2126(98)00098-7;
RA   Modis Y., Filppula S.A., Novikov D.K., Norledge B., Hiltunen J.K.,
RA   Wierenga R.K.;
RT   "The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution
RT   reveals the importance of aspartate and glutamate sidechains for
RT   catalysis.";
RL   Structure 6:957-970(1998).
CC   -!- FUNCTION: Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-
CC       trans-dienoyl-CoA.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:9739087}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Peroxisome.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
DR   EMBL; U08976; AAA82008.1; -; mRNA.
DR   EMBL; BC062226; AAH62226.1; -; mRNA.
DR   PIR; A57626; A57626.
DR   RefSeq; NP_072116.1; NM_022594.1.
DR   UniGene; Rn.6148; -.
DR   PDB; 1DCI; X-ray; 1.50 A; A/B/C=54-327.
DR   PDBsum; 1DCI; -.
DR   ProteinModelPortal; Q62651; -.
DR   SMR; Q62651; -.
DR   IntAct; Q62651; 1.
DR   MINT; MINT-4597589; -.
DR   STRING; 10116.ENSRNOP00000027537; -.
DR   SwissLipids; SLP:000001100; -.
DR   iPTMnet; Q62651; -.
DR   PhosphoSitePlus; Q62651; -.
DR   PaxDb; Q62651; -.
DR   PRIDE; Q62651; -.
DR   Ensembl; ENSRNOT00000027537; ENSRNOP00000027537; ENSRNOG00000020308.
DR   GeneID; 64526; -.
DR   KEGG; rno:64526; -.
DR   UCSC; RGD:69353; rat.
DR   CTD; 1891; -.
DR   RGD; 69353; Ech1.
DR   eggNOG; KOG1681; Eukaryota.
DR   eggNOG; ENOG410XTHX; LUCA.
DR   GeneTree; ENSGT00890000139344; -.
DR   HOGENOM; HOG000027939; -.
DR   HOVERGEN; HBG005556; -.
DR   InParanoid; Q62651; -.
DR   KO; K12663; -.
DR   OMA; SWVKDVC; -.
DR   OrthoDB; EOG091G0H26; -.
DR   PhylomeDB; Q62651; -.
DR   TreeFam; TF314317; -.
DR   UniPathway; UPA00659; -.
DR   EvolutionaryTrace; Q62651; -.
DR   PRO; PR:Q62651; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020308; -.
DR   Genevisible; Q62651; RN.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:receptor binding; IEA:Ensembl.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.12.10; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom.
DR   InterPro; IPR014748; Crontonase_C.
DR   InterPro; IPR001753; Crotonase_core_superfam.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q62651.
DR   SWISS-2DPAGE; Q62651.
KW   3D-structure; Acetylation; Complete proteome;
KW   Direct protein sequencing; Fatty acid metabolism; Isomerase;
KW   Lipid metabolism; Mitochondrion; Peroxisome; Phosphoprotein;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     33       Mitochondrion. {ECO:0000255}.
FT   CHAIN        34    327       Delta(3,5)-Delta(2,4)-dienoyl-CoA
FT                                isomerase, mitochondrial.
FT                                /FTId=PRO_0000007419.
FT   REGION      115    119       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P42126}.
FT   MOTIF       325    327       Microbody targeting signal.
FT                                {ECO:0000255}.
FT   BINDING     173    173       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:P42126}.
FT   SITE        196    196       Important for catalytic activity.
FT                                {ECO:0000305|PubMed:9417087}.
FT   SITE        204    204       Important for catalytic activity.
FT                                {ECO:0000305|PubMed:9417087}.
FT   MOD_RES     230    230       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:O35459}.
FT   MOD_RES     267    267       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13011}.
FT   MOD_RES     316    316       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:O35459}.
FT   MOD_RES     326    326       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q13011}.
FT   CONFLICT    164    164       A -> T (in Ref. 1; AAA82008).
FT                                {ECO:0000305}.
FT   STRAND       55     63       {ECO:0000244|PDB:1DCI}.
FT   STRAND       66     71       {ECO:0000244|PDB:1DCI}.
FT   HELIX        74     76       {ECO:0000244|PDB:1DCI}.
FT   HELIX        82     96       {ECO:0000244|PDB:1DCI}.
FT   STRAND      103    109       {ECO:0000244|PDB:1DCI}.
FT   HELIX       119    126       {ECO:0000244|PDB:1DCI}.
FT   HELIX       134    157       {ECO:0000244|PDB:1DCI}.
FT   STRAND      158    160       {ECO:0000244|PDB:1DCI}.
FT   STRAND      162    166       {ECO:0000244|PDB:1DCI}.
FT   STRAND      168    171       {ECO:0000244|PDB:1DCI}.
FT   HELIX       173    178       {ECO:0000244|PDB:1DCI}.
FT   STRAND      181    187       {ECO:0000244|PDB:1DCI}.
FT   STRAND      191    193       {ECO:0000244|PDB:1DCI}.
FT   HELIX       196    199       {ECO:0000244|PDB:1DCI}.
FT   HELIX       207    210       {ECO:0000244|PDB:1DCI}.
FT   HELIX       211    213       {ECO:0000244|PDB:1DCI}.
FT   HELIX       218    227       {ECO:0000244|PDB:1DCI}.
FT   STRAND      230    232       {ECO:0000244|PDB:1DCI}.
FT   HELIX       233    238       {ECO:0000244|PDB:1DCI}.
FT   STRAND      241    248       {ECO:0000244|PDB:1DCI}.
FT   HELIX       249    265       {ECO:0000244|PDB:1DCI}.
FT   HELIX       268    283       {ECO:0000244|PDB:1DCI}.
FT   HELIX       286    300       {ECO:0000244|PDB:1DCI}.
FT   HELIX       304    314       {ECO:0000244|PDB:1DCI}.
FT   HELIX       319    321       {ECO:0000244|PDB:1DCI}.
SQ   SEQUENCE   327 AA;  36172 MW;  6FAE35D7D5F66BC2 CRC64;
     MATAMTVSSK LLGLLMQQLR GTRQLYFNVS LRSLSSSAQE ASKRIPEEVS DHNYESIQVT
     SAQKHVLHVQ LNRPEKRNAM NRAFWRELVE CFQKISKDSD CRAVVVSGAG KMFTSGIDLM
     DMASDILQPP GDDVARIAWY LRDLISRYQK TFTVIEKCPK PVIAAIHGGC IGGGVDLISA
     CDIRYCTQDA FFQVKEVDVG LAADVGTLQR LPKVIGNRSL VNELTFTARK MMADEALDSG
     LVSRVFPDKD VMLNAAFALA ADISSKSPVA VQGSKINLIY SRDHSVDESL DYMATWNMSM
     LQTQDIIKSV QAAMEKKDSK SITFSKL
//

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